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AF068: Transferrin
Biochemical properties
Transferrins are eukaryotic iron-binding glycoproteins that control the level of free iron in biological fluids. The proteins evolved by duplication of a domain, each duplicated domain binding one iron atom. Members of the family include blood serotransferrin (siderophilin), milk lactotransferrin (lactoferrin), egg white ovotransferrin (conalbumin), and membrane-associated melanotransferrin [1].
Allergens from this family
Bovine lactoferrin was identified as an allergen binding IgE from 50% of cow's milk allergic patients' sera [2]. Chicken ovotransferrin (Gal d 3) is a major hen's egg allergen [3].
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References
- Lambert LA, Perri H, Halbrooks PJ, Mason AB:
Evolution of the transferrin family: conservation of residues associated with iron and anion binding.
Comp Biochem Physiol B Biochem Mol Biol 2005, 142, 129-41. [PubMed] [Full Text]
- Natale M, Bisson C, Monti G, Peltran A, Garoffo LP, Valentini S, Fabris C, Bertino E, Coscia A, Conti A:
Cow's milk allergens identification by two-dimensional immunoblotting and mass spectrometry.
Mol Nutr Food Res 2004, 48, 363-9. [PubMed] [Full Text]
- Aabin B, Poulsen LK, Ebbehoj K, Norgaard A, Frokiaer H, Bindslev-Jensen C, Barkholt V:
Identification of IgE-binding egg white proteins: comparison of results obtained by different methods.
Int Arch Allergy Immunol 1996, 109, 50-7. [PubMed]
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Links to Pfam
Family-defining Pfam domains (at least one of these domains is present in each family member):
Pfam domain |
Pfam clan |
PF00405
|
Transferrin
|
CL0177
|
Periplasmic binding protein clan
|
Links to Wikipedia
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